TIM9_ARATH
ID TIM9_ARATH Reviewed; 93 AA.
AC Q9XGX9; Q8L927; Q9SNC2;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM9;
DE AltName: Full=Protein EMBRYO DEFECTIVE 2474;
GN Name=TIM9; Synonyms=EMB2474; OrderedLocusNames=At3g46560;
GN ORFNames=F12A12.80;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10611480; DOI=10.1016/s0014-5793(99)01665-8;
RA Bauer M.F., Rothbauer U., Muehlenbein N., Smith R.J.H., Gerbitz K.-D.,
RA Neupert W., Brunner M., Hofmann S.;
RT "The mitochondrial TIM22 preprotein translocase is highly conserved
RT throughout the eukaryotic kingdom.";
RL FEBS Lett. 464:41-47(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=14730085; DOI=10.1104/pp.103.033910;
RA Lister R., Chew O., Lee M.N., Heazlewood J.L., Clifton R., Parker K.L.,
RA Millar A.H., Whelan J.;
RT "A transcriptomic and proteomic characterization of the Arabidopsis
RT mitochondrial protein import apparatus and its response to mitochondrial
RT dysfunction.";
RL Plant Physiol. 134:777-789(2004).
CC -!- FUNCTION: Mitochondrial intermembrane chaperone that participates in
CC the import and insertion of multi-pass transmembrane proteins into the
CC mitochondrial inner membrane. May also be required for the transfer of
CC beta-barrel precursors from the TOM complex to the sorting and assembly
CC machinery (SAM complex) of the outer membrane. Acts as a chaperone-like
CC protein that protects the hydrophobic precursors from aggregation and
CC guide them through the mitochondrial intermembrane space (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterohexamer; composed of 3 copies of TIM9 and 3 copies of
CC TIM10, named soluble 70 kDa complex. The complex associates with the
CC TIM22 component of the TIM22 complex. Interacts with multi-pass
CC transmembrane proteins in transit (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:14730085}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, flowers, young cotyledons and
CC leaves. {ECO:0000269|PubMed:14730085}.
CC -!- DOMAIN: The twin CX3C motif contains 4 conserved Cys residues that form
CC 2 disulfide bonds in the mitochondrial intermembrane space. However,
CC during the transit of TIM9 from cytoplasm into mitochondrion, the Cys
CC residues probably coordinate zinc, thereby preventing folding and
CC allowing its transfer across mitochondrial outer membrane (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small Tim family. {ECO:0000305}.
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DR EMBL; AF150111; AAD40017.1; -; mRNA.
DR EMBL; AL133314; CAB62326.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78172.1; -; Genomic_DNA.
DR EMBL; AY045940; AAK76614.1; -; mRNA.
DR EMBL; AY079412; AAL85143.1; -; mRNA.
DR EMBL; AY088670; AAM66992.1; -; mRNA.
DR PIR; T45593; T45593.
DR PIR; T51187; T51187.
DR RefSeq; NP_190240.1; NM_114523.5.
DR AlphaFoldDB; Q9XGX9; -.
DR SMR; Q9XGX9; -.
DR BioGRID; 9129; 1.
DR STRING; 3702.AT3G46560.1; -.
DR iPTMnet; Q9XGX9; -.
DR PaxDb; Q9XGX9; -.
DR PRIDE; Q9XGX9; -.
DR ProteomicsDB; 234357; -.
DR EnsemblPlants; AT3G46560.1; AT3G46560.1; AT3G46560.
DR GeneID; 823809; -.
DR Gramene; AT3G46560.1; AT3G46560.1; AT3G46560.
DR KEGG; ath:AT3G46560; -.
DR Araport; AT3G46560; -.
DR TAIR; locus:2075195; AT3G46560.
DR eggNOG; KOG3479; Eukaryota.
DR HOGENOM; CLU_141397_3_2_1; -.
DR InParanoid; Q9XGX9; -.
DR OMA; QDFLRMY; -.
DR OrthoDB; 1627953at2759; -.
DR PhylomeDB; Q9XGX9; -.
DR PRO; PR:Q9XGX9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9XGX9; baseline and differential.
DR Genevisible; Q9XGX9; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005758; C:mitochondrial intermembrane space; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007005; P:mitochondrion organization; IMP:TAIR.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.810; -; 1.
DR InterPro; IPR004217; Tim10-like.
DR InterPro; IPR035427; Tim10-like_dom_sf.
DR Pfam; PF02953; zf-Tim10_DDP; 1.
DR SUPFAM; SSF144122; SSF144122; 1.
PE 1: Evidence at protein level;
KW Chaperone; Disulfide bond; Metal-binding; Mitochondrion; Protein transport;
KW Reference proteome; Translocation; Transport; Zinc.
FT CHAIN 1..93
FT /note="Mitochondrial import inner membrane translocase
FT subunit TIM9"
FT /id="PRO_0000193605"
FT MOTIF 43..67
FT /note="Twin CX3C motif"
FT DISULFID 43..67
FT /evidence="ECO:0000250"
FT DISULFID 47..63
FT /evidence="ECO:0000250"
FT CONFLICT 35
FT /note="M -> L (in Ref. 5; AAM66992)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="V -> F (in Ref. 1; AAD40017)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="A -> S (in Ref. 1; AAD40017)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 93 AA; 10715 MW; 50B1ED87E64DE8BE CRC64;
MDASMMAGLD GLPEEDKAKM ASMIDQLQLR DSLRMYNSLV ERCFVDCVDS FTRKSLQKQE
ETCVMRCAEK FLKHTMRVGM RFAELNQNAP TQD
